Dysregulated phosphorylation and nuclear translocation of cyclic AMP response element binding protein (CREB) in rat liver after chronic ethanol binge

2012 ◽  
Vol 679 (1-3) ◽  
pp. 101-108 ◽  
Author(s):  
Annayya R. Aroor ◽  
Daniel E. Jackson ◽  
Shivendra D. Shukla
Keyword(s):  
Cyclic Amp ◽  
Rat Liver ◽  
Nuclear Translocation ◽  
Binding Protein ◽  
Chronic Ethanol ◽  
Response Element ◽  
Element Binding Protein ◽  
Cyclic Amp Response Element

scholarly journals Mitochondrial Cyclic AMP Response Element-binding Protein (CREB) Mediates Mitochondrial Gene Expression and Neuronal Survival

2005 ◽  
Vol 280 (49) ◽  
pp. 40398-40401 ◽  
Author(s):  
Junghee Lee ◽  
Chun-Hyung Kim ◽  
David K. Simon ◽  
Lyaylya R. Aminova ◽  
Alexander Y. Andreyev ◽  
...  
Keyword(s):  
Gene Expression ◽  
Cyclic Amp ◽  
Neuronal Survival ◽  
Binding Protein ◽  
Mitochondrial Gene ◽  
Mitochondrial Gene Expression ◽  
Response Element ◽  
Element Binding Protein ◽  
Cyclic Amp Response Element

A cDNA for a human cyclic AMP response element-binding protein which is distinct from CREB and expressed preferentially in brain

1990 ◽  
Vol 10 (4) ◽  
pp. 1347-1357
Author(s):  
C J Kara ◽  
H C Liou ◽  
L B Ivashkiv ◽  
L H Glimcher
Keyword(s):  
Dna Binding ◽  
Cyclic Amp ◽  
Leucine Zipper ◽  
Binding Protein ◽  
Structural Similarity ◽  
Response Element ◽  
Cellular Genes ◽  
Viral Promoters ◽  
Element Binding Protein ◽  
Cyclic Amp Response Element

The cyclic AMP response element (CRE) is found in many cellular genes regulated by cyclic AMP, and similar elements are present in the early genes of adenovirus that are activated by E1A. The transcription factor CREB has previously been shown to bind this site, and cDNAs for CREB have recently been characterized. We report here the isolation of a cDNA encoding a human DNA-binding protein that also recognizes this motif in cellular and viral promoters. This protein, HB16, displays structural similarity to CREB and to c-Jun and c-Fos, which bind the related 12-O-tetradecanoylphorbol-13-acetate response element (TRE). HB16 contains a highly basic, putative DNA-binding domain and a leucine zipper structure thought to be involved in dimerization. Deletional analysis of HB16 demonstrated that the leucine zipper is required for its interaction with DNA. In addition, HB16 could form a complex with c-Jun but not with c-Fos. Despite its structural similarity to c-Jun and c-Fos and its interaction with c-Jun, HB16 had approximately a 10-fold-lower affinity for the TRE sequence than for the CRE sequence. Although HB16 and CREB both recognized the CRE motif, an extensive binding analysis of HB16 revealed differences in the fine specificity of binding of the two proteins. HB16 mRNA was found at various levels in many human tissues but was most abundant in brain, where its expression was widespread. The existence of more than one CRE-binding protein suggests that the CRE motif could serve multiple regulatory functions.

scholarly journals A cDNA for a human cyclic AMP response element-binding protein which is distinct from CREB and expressed preferentially in brain.

1990 ◽  
Vol 10 (4) ◽  
pp. 1347-1357 ◽  
Author(s):  
C J Kara ◽  
H C Liou ◽  
L B Ivashkiv ◽  
L H Glimcher
Keyword(s):  
Dna Binding ◽  
Cyclic Amp ◽  
Leucine Zipper ◽  
Binding Protein ◽  
Structural Similarity ◽  
Response Element ◽  
Cellular Genes ◽  
Viral Promoters ◽  
Element Binding Protein ◽  
Cyclic Amp Response Element

The cyclic AMP response element (CRE) is found in many cellular genes regulated by cyclic AMP, and similar elements are present in the early genes of adenovirus that are activated by E1A. The transcription factor CREB has previously been shown to bind this site, and cDNAs for CREB have recently been characterized. We report here the isolation of a cDNA encoding a human DNA-binding protein that also recognizes this motif in cellular and viral promoters. This protein, HB16, displays structural similarity to CREB and to c-Jun and c-Fos, which bind the related 12-O-tetradecanoylphorbol-13-acetate response element (TRE). HB16 contains a highly basic, putative DNA-binding domain and a leucine zipper structure thought to be involved in dimerization. Deletional analysis of HB16 demonstrated that the leucine zipper is required for its interaction with DNA. In addition, HB16 could form a complex with c-Jun but not with c-Fos. Despite its structural similarity to c-Jun and c-Fos and its interaction with c-Jun, HB16 had approximately a 10-fold-lower affinity for the TRE sequence than for the CRE sequence. Although HB16 and CREB both recognized the CRE motif, an extensive binding analysis of HB16 revealed differences in the fine specificity of binding of the two proteins. HB16 mRNA was found at various levels in many human tissues but was most abundant in brain, where its expression was widespread. The existence of more than one CRE-binding protein suggests that the CRE motif could serve multiple regulatory functions.

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